Characterization of a highly toxic, large molecular size heat‐stable enterotoxin produced by a clinical isolate of Yersinia enterocolitica

FEBS Letters

Takeda, Tae¹  Murata, Hiroshi²  Nakao, Hiroshi¹  Yoshino, Ken-ichi²  Shimonishi, Yasutsugu²  Takao, Toshifumi²  Huang, Xiaozhe¹ 

[1] Department of Infectious Diseases Research, National Children's Medical Research Center, Taishido 3-35-31, Setagaya-ku, Tokyo 154, Japan;Institute for Protein Research, Osaka University, Yamadaoka 3-2, Suita, Osaka 565, Japan

关键词: Heat-stable enterotoxin;    Amino acid sequence;    Purification;    Pro-sequence;    Yersinia enterocolitica;   

DOI  :  10.1016/0014-5793(95)00267-D

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A novel heat-stable enterotoxin (ST) designated as Y-STc was purified to homogeneity from the culture supernatant of a pathogenic strain of Yersinia enterocolitica serotype O3 and its amino acid sequence was determined. The mature Y-STc was found to consist of 53 amino acid residues, which includes the putative pro-sequence. The molecular weight of Y-STc was 5683 and constituted the largest molecular size in the family of currently known STs. The minimum effective dose of purified Y-STc in the suckling mouse assay was 0.6 ng (0.1 pmol), indicating that, despite the long sequence, Y-STc is the most toxic in the ST family.

【 授权许可】

Unknown